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methyl (S)-2-(2-(4-bromophenylcarbamoyl)pyrrolidine-1-carbonyl)phenylcarbamate is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

1401065-87-9

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1401065-87-9 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 1401065-87-9 includes 10 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 7 digits, 1,4,0,1,0,6 and 5 respectively; the second part has 2 digits, 8 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 1401065-87:
(9*1)+(8*4)+(7*0)+(6*1)+(5*0)+(4*6)+(3*5)+(2*8)+(1*7)=109
109 % 10 = 9
So 1401065-87-9 is a valid CAS Registry Number.

1401065-87-9Relevant academic research and scientific papers

Ester vs. amide on folding: A case study with a 2-residue synthetic peptide

Vijayadas, Kuruppanthara N.,Nair, Roshna V.,Gawade, Rupesh L.,Kotmale, Amol S.,Prabhakaran, Panchami,Gonnade, Rajesh G.,Puranik, Vedavadi G.,Rajamohanan, Pattuparambil R.,Sanjayan, Gangadhar J.

, p. 8348 - 8356 (2013)

Although known for their inferiority as hydrogen-bonding acceptors when compared to amides, esters are often found at the C-terminus of peptides and synthetic oligomers (foldamers), presumably due to the synthetic readiness with which they are obtained using protected peptide coupling, deploying amino acid esters at the C-terminus. When the H-bonding interactions deviate from regularity at the termini, peptide chains tend to "fray apart". However, the individual contributions of C-terminal esters in causing peptide chain end-fraying goes often unnoticed, particularly due to diverse competing effects emanating from large peptide chains. Herein, we describe a striking case of a comparison of the individual contributions of C-terminal ester vs. amide carbonyl as a H-bonding acceptor in the folding of a peptide. A simple two-residue peptide fold has been used as a testing case to demonstrate that amide carbonyl is far superior to ester carbonyl in promoting peptide folding, alienating end-fraying. This finding would have a bearing on the fundamental understanding of the individual contributions of stabilizing/destabilizing non-covalent interactions in peptide folding.

An unusual conformational similarity of two peptide folds featuring sulfonamide and carboxamide on the backbone

Vijayadas, Kuruppanthara N.,Davis, Hilda C.,Kotmale, Amol S.,Gawade, Rupesh L.,Puranik, Vedavadi G.,Rajamohanan, Pattuparambil R.,Sanjayan, Gangadhar J.

, p. 9747 - 9749 (2012/10/29)

Two folded peptides featuring carboxamide and sulfonamide at the core of the peptide fold have been shown to possess almost similar conformational features, despite the well-known fact that carboxamides and sulfonamides have strikingly different hydrogen-

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